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Protein monoubiquitination and polyubiquitination generate structural diversity to control distinct biological processes

Ubiquitination involves the attachment of ubiquitin (Ub) to lysine residues on substrate proteins or itself, which can result in protein monoubiquitination or polyubiquitination. Polyubiquitination through different lysines (seven) or the N‐terminus of Ub can generate different protein‐Ub structures...

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Published in:IUBMB life 2012-02, Vol.64 (2), p.136-142
Main Authors: Sadowski, Martin, Suryadinata, Randy, Tan, Anthonius Ricardo, Roesley, Siti Nur Ain, Sarcevic, Boris
Format: Article
Language:English
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Summary:Ubiquitination involves the attachment of ubiquitin (Ub) to lysine residues on substrate proteins or itself, which can result in protein monoubiquitination or polyubiquitination. Polyubiquitination through different lysines (seven) or the N‐terminus of Ub can generate different protein‐Ub structures. These include monoubiquitinated proteins, polyubiqutinated proteins with homotypic chains through a particular lysine on Ub or mixed polyubiquitin chains generated by polymerization through different Ub lysines. The ability of the ubiquitination pathway to generate different protein‐Ub structures provides versatility of this pathway to target proteins to different fates. Protein ubiquitination is catalyzed by Ub‐conjugating and Ub‐ligase enzymes, with different combinations of these enzymes specifying the type of Ub modification on protein substrates. How Ub‐conjugating and Ub‐ligase enzymes generate this structural diversity is not clearly understood. In the current review, we discuss mechanisms utilized by the Ub‐conjugating and Ub‐ligase enzymes to generate structural diversity during protein ubiquitination, with a focus on recent mechanistic insights into protein monoubiquitination and polyubiquitination. © IUBMB, IUBMB Life, 2011.
ISSN:1521-6543
1521-6551
DOI:10.1002/iub.589